Extended Data Fig. 3: Helix α14 of LnaB is important for its interaction with actin.
From: Structure and mechanism of an actin-dependent bacterial phosphoryl AMPylase
a–c, Detailed views of LnaB interacting with actin as shown in Fig. 2a. Hydrogen bonds are shown in blue dashed lines. d, Structural superposition of LnaB: actin binary complex with other actin complexes by αC atoms from actin. Actin is showed in grey ribbon and its subdomains are numbered. The actin-binding helixes are shown as cylindrical cartoon. e, Sequence alignment of the LxER motif in helix α14 of LnaB with other actin-binding proteins. Identities and similarities are highlighted in red, in green, respectively. f, Region of residues 361–369 in helix α14 is required for LnaB activation. The data represent three independent experiments. g, Detailed view of the ATP-binding pocket within actin. The ATP is depicted in gray stick with an annealing omit map encountered at 2.0σ. The residues Q137 and D154 that are necessary to ATPase activity were displayed by yellow sticks. h, Evaluation of effect of the ATPase activity of actin on its activation of LnaB. The data represent three independent experiments.
